Analytical Data
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Gene name
BRAP
- Application
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Alternative Names
BRAP；RNF52；BRCA1-associated Protein
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
J3KNN7
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Expression Region
1-562aa
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AA Sequence
MSDEEIKKTTLASAVACLEGKSPGEKVAIIHQHLGRREMTDVIIETMKSNPDELKTTVEERKSSEASPTAQRSKDHSKECINAAPDSPSKQLPDQISFFSGNPSVEIVHGIMHLYKTNKMTSLKEDVRRSAMLCILTVPAAMTSHDLMKFVAPFNEVIEQMKIIRDSTPNQYMVLIKFRAQADADSFYMTCNGRQFNSIEDDVCQLVYVERAEVLKSEDGASLPVMDLTELPKCTVCLERMDESVNGILTTLCNHSFHSQCLQRWDDTTCPVCRYCQTPEPVEENKCFECGVQENLWICLICGHIGCGRYVSRHAYKHFEETQHTYAMQLTNHRVWDYAGDNYVHRLVASKTDGKIVQYECEGDTCQEEKIDALQLEYSYLLTSQLESQRIYWENKIVRIEKDTAEEINNMKTKFKETIEKCDNLEHKLNDLLKEKQSVERKCTQLNTKVAKLTNELKEEQEMNKCLRANQVLLQNKLKEEERVLKETCDQKDLQITEIQEQLRDVMFYLETQQKINHLPAETRQEIQEGQINIAMASASSPASSGGSGKLPSRKGRSKRGK
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Molecular Weight
64.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
BRAP (BRCA1-A/B RING domain protein) is an important component in cellular pathways related to cancer and DNA repair mechanisms. It functions as an E3 ubiquitin ligase and plays a crucial role in the regulation of protein stability and degradation, impacting cell cycle progression and apoptotic responses. The investigation of BRAP has gained momentum due to its association with various cancers, particularly breast cancer, where mutations or dysregulation can lead to tumorigenesis. Researchers are exploring BRAP's role in modulating the stability of key proteins involved in DNA damage response, thereby elucidating its potential as a therapeutic target. Moreover, BRAP is implicated in the regulation of the NF-kB signaling pathway, contributing to inflammation and cancer progression. The study of BRAP and its reconstituted protein forms aims to provide insights into its structure-function relationships, enhancing our understanding of its role in cellular homeostasis and disease mechanisms. This research not only seeks to unravel the underlying molecular pathways but also aims to exploit BRAP’s functions for the development of targeted therapies that could improve clinical outcomes in cancer treatment. Overall, the study of BRAP reconstituted proteins stands at the intersection of cancer biology and therapeutic innovation, promising to yield valuable knowledge that could lead to novel interventions in cancer therapy.
